Transcription Factor
| Accessions: | ECK120008623 (RegulonDB 7.5) |
| Names: | AgaR, AgaR DNA-binding transcriptional repressor |
| Organisms: | ECK12 |
| Libraries: | RegulonDB 7.5 1 1 Salgado H, Peralta-Gil M, Gama-Castro S, Santos-Zavaleta A, Muniz-Rascado L, Garcia-Sotelo JS, Weiss V, Solano-Lira H, Martinez-Flores I, Medina-Rivera A, Salgado-Osorio G, Alquicira-Hernandez S, Alquicira-Hernandez K, Lopez-Fuentes A, Porron-Sotelo L, Huerta AM, Bonavides-Martinez C, Balderas-Martinez YI, Pannier L, Olvera M, Labastida A, Jimenez-Jacinto V, Vega-Alvarado L, Del Moral-Chavez V, Hernandez-Alvarez A, Morett E, Collado-Vides J. RegulonDB v8.0: omics data sets, evolutionary conservation, regulatory phrases, cross-validated gold standards and more. Nucleic Acids Res. 2013 Jan 1;41(D1):D203-D213. [Pubmed] |
| Notes: | N-acetylgalactosamine repressor, AgaR, negatively controls the expression of the aga gene cluster, which is involved in transport and catabolism of N-acetylgalactosamine and d-galactosamine Ray WK,2004; Brinkkotter A,2000 It is negatively autoregulated and coordinately represses transcription of the divergent agaZVWEFA operon, which is related to transport and degradation of N-acetylgalactosamine Ray WK,2004 This repressor responds to N-acetylgalactosamine and d-galactosamine in the medium.As a member of the DeoR/GlpR family of transcriptional regulators Ray WK,2004 AgaR features an N-terminal domain containing a helix-turn-helix motif and a C-terminal domain that includes the key residues involved in co-inducer recognition and oligomerization Ray WK,2004 In accordance with other helix-turn-helix DNA-binding repressors, AgaR may bind to DNA as a tetramer; AgaR binds in tandem to several repeat sequences in the intergenic regions of agaZp, agaRp, and agaSp to repress transcription by overlapping the - 35 and -10 boxes; The binding targets for AgaR consist of 24-nucleotide-long repeat sequences that possess conserved motifs Ray WK,2004agaR: N-acetylglactosamine degradation Reizer J,1996; repressor; Transcription related; amino sugar conversions; regulation of transcription, DNA-dependent; intracellular; sequence-specific DNA binding transcription factor activity; DNA binding; transcription, DNA-dependent |
| Length: | 270 |
| Pfam Domains: | 18-74 DeoR-like helix-turn-helix domain 18-64 HTH domain 88-247 DeoR C terminal sensor domain |
| Sequence: (in bold interface residues) | 1 MSNTDASGEKRVTGTSERREQIIQRLRQQGSVQVNDLSALYGVSTVTIRNDLAFLEKQGI 60 61 AVRAYGGALICDSTTPSVEPSVEDKSALNTAMKRSVAKAAVELIQPGHRVILDSGTTTFE 120 121 IARLMRKHTDVIAMTNGMNVANALLEAEGVELLMTGGHLRRQSQSFYGDQAEQSLQNYHF 180 181 DMLFLGVDAIDLERGVSTHNEDEARLNRRMCEVAERIIVVTDSSKFNRSSLHKIIDTQRI 240 241 DMIIVDEGIPADSLEGLRKAGVEVILVGE* |
| Interface Residues: | 44, 46, 47, 49, 50, 109, 110 |
| 3D-footprint Homologues: | 4a12_B, 8df8_A |
| Binding Motifs: | AgaR CTTTCrTTTyvTTTykwTT |
| Binding Sites: | ECK120012517 ECK120012519 ECK120012521 ECK120012525 ECK120012527 ECK120012529 ECK120012531 ECK120012533 ECK120012535 ECK120015699 ECK120015701 |
| Publications: | Ray WK., Larson TJ. Application of AgaR repressor and dominant repressor variants for verification of a gene cluster involved in N-acetylgalactosamine metabolism in Escherichia coli K-12. Mol Microbiol. 51(3):813-26 (2004). [Pubmed] Brinkkotter A., Kloss H., Alpert C., Lengeler JW. Pathways for the utilization of N-acetyl-galactosamine and galactosamine in Escherichia coli. Mol Microbiol. 37(1):125-35 (2000). [Pubmed] Reizer J., Ramseier TM., Reizer A., Charbit A., Saier MH. Novel phosphotransferase genes revealed by bacterial genome sequencing: a gene cluster encoding a putative N-acetylgalactosamine metabolic pathway in Escherichia coli. Microbiology. 142 ( Pt 2):231-50 (1996). [Pubmed] |
| Related annotations: | PaperBLAST |
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